Information System for Tracking Study Results

Hlavním cílem této bakalářské práce je navrhnout a implementovat informační systém pro správu a evidenci studijních výsledků doktorandů. Tento systém je uzpůsoben pro snadnou správu studentů a učitelů, z nichž je poté vytvořen rozvrh prezentací každého studenta a jejich výkon následně i oznámkován. Při jeho vývoji byl použit PHP framework Nette a CSS framework Bootstrap . Systém nahrazuje současný způsob tvorby rozvrhu a evidenci známek, který byl řešen Excel dokumentem.The main goal of this bachelor thesis is design and implementation of information system for Tracking study results of doctoral candidates . This system is made for easy student and teacher management, from which the schedule for student presentations is made and their performance graded afterwards . During the development , the PHP Nette framework and the CSS Bootstrap framework were used . System is replacing current way of schedule creating and grade records , which solution was Excel document.

Structural and functional insight into human O-GlcNAcase.

O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value

Insights into O-Linked N-Acetylglucosamine ([0-9]O-GlcNAc) Processing and Dynamics through Kinetic Analysis of O-GlcNAc Transferase and O-GlcNAcase Activity on Protein Substrates*

Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA). To quantitatively address the activity of these enzymes on protein substrates, we generated five structurally diverse proteins in both unmodified and O-GlcNAc-modified states. We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein. Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels. This was supported by the observation that K(m,app) values for UDP-GlcNAc varied considerably (from 1 μM to over 20 μM), depending on the protein substrate, suggesting that some OGT substrates will be nutrient-responsive, whereas others are constitutively modified. The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors. We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells. These studies provide kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity

Design, Creation and Implementation of Software Applications in the Corporate Environment

Hlavním cílem této práce je navrhnout a implementovat informační systém Dropohs do firemního prostředí, který bude vytvářet a spravovat eshopy, které budou automaticky komunikovat se službou Dropshipping pro autonomní řešení objednávek a jejich distribuci. Dalším cílem bude tento systém analyzovat po spuštění do reálného prostředí. Tento systém byl vytvořen za pomocí PHP frameworku na bázi modelu MVC.The main goal of this thesis is design and implement information system Dropohs into business environment, that will create and manage eshops, which will automatically communicate with online service Dropshipping for autonomous solution of orders and their distribution. Next goal will be to analyze this system after running it in real environment. This system was made with MVC based PHP framework.

The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha.

Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of intracellular glycosylation catalyzed by the conserved O-linked GlcNAc transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide (TPR) repeats that mediates the recognition of a broad range of target proteins. Components of the nuclear pore complex are major OGT targets, as OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc modification at the nuclear envelope. To gain insight into the mechanism of target recognition, we solved the crystal structure of the homodimeric TPR domain of human OGT, which contains 11.5 TPR repeats. The repeats form an elongated superhelix. The concave surface of the superhelix is lined by absolutely conserved asparagines, in a manner reminiscent of the peptide-binding site of importin alpha. Based on this structural similarity, we propose that OGT uses an analogous molecular mechanism to recognize its targets

Molecular recognition:O-GlcNAc transfer: size matters

O-GlcNAc transferase is an essential protein catalyzing the O-GlcNAc modification of hundreds of intracellular proteins in higher eukaryotes. The structure of human O-GlcNAc transferase represents a leap in our understanding of the catalytic mechanism and recognition of protein substrates